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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Burakova L.P., Krasitskaya V.V., Kudryavtsev A.N., Shimomura O..., Frank L.A.
Заглавие : Hydrogen-bond networks between the C-terminus and Arg from the first alpha-helix stabilize photoprotein molecules
Колич.характеристики :7 с
Коллективы : RFBR [12-04-00753-a]; Government of Russian Federation [11.G34.31.0058]
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2014. - Vol. 13, Is. 3. - С. 541-547. - ISSN 1474-905X, DOI 10.1039/c3pp50369k. - ISSN 1474-9092
Примечания : Cited References: 22. - The work was supported by RFBR grant 12-04-00753-a, by the Program of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058).
Предметные рубрики: GREEN FLUORESCENT PROTEIN
CA2+-REGULATED PHOTOPROTEIN
BIOLUMINESCENT IMMUNOASSAY
COELENTERAZINE BINDING
ANGSTROM RESOLUTION
ENERGY-TRANSFER
FUSION PROTEIN
APO-OBELIN
AEQUORIN
EXPRESSION
Аннотация: Previous studies have stated that aequorin loses most of its bioluminescence activity upon modification of the C-terminus, thus limiting the production of photoprotein fusion proteins at its N-terminus. In the present work, we investigate the importance of the C-terminal proline and the hydrogen bonds it forms for photoprotein active complex formation, stability and functional activity. According to the crystal structures of obelin and aequorin, two Ca2+-regulated photoproteins, the carboxyl group of the C-terminal Pro forms two hydrogen bonds with the side chain of Arg21 (Arg15 in aequorin case) situated in the first a-helix. Whereas, deletion or substitution of the C-terminal proline could noticeably change the bioluminescence activity, stability or the yield of an active photoprotein complex. Therefore, modifications of the first alpha-helix Arg has a clear destructive effect on the main photoprotein properties. A C-terminal hydrogen-bond network is proposed to be important for the stability of photoprotein molecules towards external disturbances, when taking part in the formation of locked protein conformations and isolation of coelenterazine-binding cavities.
WOS
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova L. P., Eremeeva E. V., Vysotski E. S.
Заглавие : The interaction of C-terminal Tyr208 and Tyr13 of the first α-helix ensures a closed conformation of ctenophore photoprotein berovin
Место публикации : Photochem. Photobiol. Sci. - 2020. - Vol. 19, Is. 3. - С. 313-323. - ISSN 1474905X (ISSN), DOI 10.1039/c9pp00436j
Аннотация: Light-sensitive Ca2+-regulated photoprotein berovin is responsible for the bioluminescence of the ctenophore Beroe abyssicola. It shares many properties of hydromedusan photoproteins although the degree of identity of its amino acid sequence with those of photoproteins is low. There is a hydrogen bond between C-terminal Pro and Arg situated in the N-terminal ?-helix of hydromedusan photoproteins that supports a closed conformation of the internal cavity of the photoprotein molecule with bound 2-hydroperoxycoelenterazine. The C- and N-terminal hydrogen bond network is necessary to properly isolate the photoprotein active site from the solvent and consequently to provide a high quantum yield of the bioluminescence reaction. In order to find out which berovin residues perform the same function we modified the N- and C-termini of the protein by replacing or deleting various amino acid residues. The studies on berovin mutants showed that the interaction between C-terminal Tyr208 and Tyr13 localized in the first ?-helix of the photoprotein is important for the stabilization and proper orientation of the oxygenated coelenterazine adduct within the internal cavity as well as for supporting the closed photoprotein conformation. We also suggest that the interplay between Tyr residues in ctenophore photoproteins occurs rather through the ?-? interaction of their phenyl rings than through hydrogen bonds as in hydromedusan photoproteins. This journal is © The Royal Society of Chemistry and Owner Societies.
Scopus
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Malikova N.P., Stepanyuk G.A., Frank L.A., Markova S.V., Vysotski E.S., Lee J...
Заглавие : Spectral tuning of obelin bioluminescence by mutations of Trp92
Колич.характеристики :5 с
Место публикации : FEBS Lett.: ELSEVIER SCIENCE BV, 2003. - Vol. 554, Is. 01.02.2013. - С. 184-188. - ISSN 0014-5793, DOI 10.1016/S0014-5793(03)01166-9
Примечания : Cited References: 13
Предметные рубрики: VIOLET BIOLUMINESCENCE
W92F OBELIN
AEQUORIN
PURIFICATION
EXPRESSION
EMISSION
CLONING
Ключевые слова (''Своб.индексиров.''): photoprotein--aequorin--calcium--fluorescence
Аннотация: The Ca2+-regulated photoprotein obelin was substituted at Trp92 by His, Lys, Glu, and Arg. All mutants fold into stable conformations and produce bimodal bioluminescence spectra with enhanced contribution from a violet emission. The W92R mutant has an almost monomodal bioluminescence (lambda(max)=390 nm) and monomodal fluorescence (lambda(max)=425 nm) of the product. Results are interpreted by an excited state proton transfer mechanism involving the substituent side group and His22 in the binding cavity. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Liu Z.J., Stepanyuk G.A., Vysotski E.S., Lee J..., Markova S.V., Malikova N.P., Wang B.C.
Заглавие : Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state
Колич.характеристики :6 с
Место публикации : Proc. Natl. Acad. Sci. U. S. A.: NATL ACAD SCIENCES, 2006. - Vol. 103, Is. 8. - С. 2570-2575. - ISSN 0027-8424, DOI 10.1073/pnas.0511142103
Примечания : Cited References: 51
Предметные рубрики: X-RAY-DIFFRACTION
ANGSTROM RESOLUTION
CA2+-REGULATED PHOTOPROTEINS
AEQUORIN BIOLUMINESCENCE
VIOLET BIOLUMINESCENCE
W92F OBELIN
PROTEIN
LUCIFERASE
LIGHT
PROGRAM
Ключевые слова (''Своб.индексиров.''): coelenterazine--photoprotein--ef hand--luciferase--aequorin
Аннотация: The crystal structure at 1.93-angstrom resolution is determined for the Ca2+-discharged obelin containing three bound calcium ions as well as the product of the bioluminescence reaction, coelenteramide. This finding extends the series of available spatial structures of the ligand-dependent conformations of the protein to four, the obelin itself, and those after the bioluminescence reaction with or without bound Ca2+ and/or coelenteramide. Among these structures, global conformational changes are small, typical of the class of "calcium signal modulators" within the EF-hand protein superfamily. Nevertheless, in the active site there are significant repositions of two residues. The His-175 imidazole ring flips becoming almost perpendicular to the original orientation corroborating the crucial importance of this residue for triggering bioluminescence. Tyr-138 hydrogen bonded to the coelenterazine N1-atom in unreacted obelin is moved away from the binding cavity after reaction. However, this Tyr is displaced by a water molecule from within the cavity, which now forms a hydrogen bond to the same atom, the amide N of coelenteramide. From this observation, a reaction scheme is proposed that would result in the neutral coelenteramide as the primary excited state product in photoprotein bioluminescence. From such a higher energy state it is now energetically feasible to account for the shorter wavelength bioluminescence spectra obtained from some photoprotein mutants or to populate the lower energy state of the phenolate anion to yield the blue bioluminescence ordinarily observed from native photoproteins.
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